The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112

N6-methyladenosine (m6A) has recently been found abundantly on messenger RNA and shown to regulate most steps of mRNA metabolism. Several important m6A methyltransferases have been described functionally and structurally, but the enzymes responsible for installing one m6A residue on each subunit of human ribosomes at functionally important sites have eluded identification for over 30 years. Here, we identify METTL5 as the enzyme responsible for 18S rRNA m6A modification and confirm ZCCHC4 as the 28S rRNA modification enzyme. We show that METTL5 must form a heterodimeric complex with TRMT112, a known methyltransferase activator, to gain metabolic stability in cells. We provide the first atomic resolution…

• PI
  Pacific Institute for Climate Solutions

  Award: PICS07484
• DF
  Deutsche Forschungsgemeinschaft

  Award: SPP1784: BO3442/2-2
• FD
  Fonds De La Recherche Scientifique - FNRS

  Award: CDR J.0095.19-33696322
• CN
  Centre National de la Recherche Scientifique
• NI
  National Institutes of Health

  Awards: NS111631, CA186702
• WC
  Weill Cornell Medical College